Calponin binds G-actin and F-actin with similar affinity
Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affi...
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| Veröffentlicht in: | FEBS letters 2006-09, Vol.580 (20), p.4801-4806 |
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| container_title | FEBS letters |
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| creator | Ferjani, Imen Fattoum, Abdellatif Maciver, Sutherland K. Manai, Mohamed Benyamin, Yves Roustan, Claude |
| description | Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affinity (
K
d of 0.15
μM). We show that the arrangement of binding is similar to that of F-actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29
Å when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin. |
| doi_str_mv | 10.1016/j.febslet.2006.07.065 |
| format | Article |
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K
d of 0.15
μM). We show that the arrangement of binding is similar to that of F-actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29
Å when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2006.07.065</identifier><identifier>PMID: 16901482</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Actin ; Actins - metabolism ; Animals ; Binding Sites ; Calcium-Binding Proteins - metabolism ; Calponin ; calponin homology domain ; Calponins ; Cell signalling ; Cysteine - metabolism ; Cytoskeleton ; ELISA ; enzyme-linked immunosorbant sandwich assay ; ERK ; extracellular regulated kinase ; Fluorescent Dyes - metabolism ; Microfilament Proteins - metabolism ; Muscle Proteins - metabolism ; Muscle, Smooth - metabolism ; PKC ; Protein Binding ; protein kinase C ; Rabbits ; Spectrometry, Fluorescence</subject><ispartof>FEBS letters, 2006-09, Vol.580 (20), p.4801-4806</ispartof><rights>2006 Federation of European Biochemical Societies</rights><rights>FEBS Letters 580 (2006) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4285-7369f2559129be09e0602336a7a49a19ca0aef2f290dea292ad284e8c1a066ee3</citedby><cites>FETCH-LOGICAL-c4285-7369f2559129be09e0602336a7a49a19ca0aef2f290dea292ad284e8c1a066ee3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2006.07.065$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579306009215$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16901482$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferjani, Imen</creatorcontrib><creatorcontrib>Fattoum, Abdellatif</creatorcontrib><creatorcontrib>Maciver, Sutherland K.</creatorcontrib><creatorcontrib>Manai, Mohamed</creatorcontrib><creatorcontrib>Benyamin, Yves</creatorcontrib><creatorcontrib>Roustan, Claude</creatorcontrib><title>Calponin binds G-actin and F-actin with similar affinity</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affinity (
K
d of 0.15
μM). We show that the arrangement of binding is similar to that of F-actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29
Å when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin.</description><subject>Actin</subject><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Calponin</subject><subject>calponin homology domain</subject><subject>Calponins</subject><subject>Cell signalling</subject><subject>Cysteine - metabolism</subject><subject>Cytoskeleton</subject><subject>ELISA</subject><subject>enzyme-linked immunosorbant sandwich assay</subject><subject>ERK</subject><subject>extracellular regulated kinase</subject><subject>Fluorescent Dyes - metabolism</subject><subject>Microfilament Proteins - metabolism</subject><subject>Muscle Proteins - metabolism</subject><subject>Muscle, Smooth - metabolism</subject><subject>PKC</subject><subject>Protein Binding</subject><subject>protein kinase C</subject><subject>Rabbits</subject><subject>Spectrometry, Fluorescence</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1PwzAMhiMEYmPwE0A9cWtx0jZNTgimfSBN4gCcozR1RaauHU3HtH9PqlbiCCfb8uvX9kPILYWIAuUP26jE3FXYRQyAR5BFwNMzMqUii8M44eKcTAFoEqaZjCfkyrkt-FpQeUkmlEvfEmxKxFxX-6a2dZDbunDBKtSm85Wui2A55kfbfQbO7myl20CXpa1td7omF6WuHN6McUY-lov3-TrcvK5e5k-b0CRMpGEWc1myNJWUyRxBInBgccx1phOpqTQaNJasZBIK1EwyXTCRoDBUA-eI8YzcD777tvk6oOvUzjqDVaVrbA5OcZEJkcTCC9NBaNrGuRZLtW_tTrcnRUH1yNRWjchUj0xBpjwyP3c3LjjkOyx-p0ZGXrAeBEdb4el_rmq5eGZvPf8ev_8ZJKP9rsfBCj2xb4utcsZibbCwLZpOFY3949of3bCTaw</recordid><startdate>20060904</startdate><enddate>20060904</enddate><creator>Ferjani, Imen</creator><creator>Fattoum, Abdellatif</creator><creator>Maciver, Sutherland K.</creator><creator>Manai, Mohamed</creator><creator>Benyamin, Yves</creator><creator>Roustan, Claude</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20060904</creationdate><title>Calponin binds G-actin and F-actin with similar affinity</title><author>Ferjani, Imen ; Fattoum, Abdellatif ; Maciver, Sutherland K. ; Manai, Mohamed ; Benyamin, Yves ; Roustan, Claude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4285-7369f2559129be09e0602336a7a49a19ca0aef2f290dea292ad284e8c1a066ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Actin</topic><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Calponin</topic><topic>calponin homology domain</topic><topic>Calponins</topic><topic>Cell signalling</topic><topic>Cysteine - metabolism</topic><topic>Cytoskeleton</topic><topic>ELISA</topic><topic>enzyme-linked immunosorbant sandwich assay</topic><topic>ERK</topic><topic>extracellular regulated kinase</topic><topic>Fluorescent Dyes - metabolism</topic><topic>Microfilament Proteins - metabolism</topic><topic>Muscle Proteins - metabolism</topic><topic>Muscle, Smooth - metabolism</topic><topic>PKC</topic><topic>Protein Binding</topic><topic>protein kinase C</topic><topic>Rabbits</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ferjani, Imen</creatorcontrib><creatorcontrib>Fattoum, Abdellatif</creatorcontrib><creatorcontrib>Maciver, Sutherland K.</creatorcontrib><creatorcontrib>Manai, Mohamed</creatorcontrib><creatorcontrib>Benyamin, Yves</creatorcontrib><creatorcontrib>Roustan, Claude</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ferjani, Imen</au><au>Fattoum, Abdellatif</au><au>Maciver, Sutherland K.</au><au>Manai, Mohamed</au><au>Benyamin, Yves</au><au>Roustan, Claude</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calponin binds G-actin and F-actin with similar affinity</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2006-09-04</date><risdate>2006</risdate><volume>580</volume><issue>20</issue><spage>4801</spage><epage>4806</epage><pages>4801-4806</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affinity (
K
d of 0.15
μM). We show that the arrangement of binding is similar to that of F-actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29
Å when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>16901482</pmid><doi>10.1016/j.febslet.2006.07.065</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Actin Actins - metabolism Animals Binding Sites Calcium-Binding Proteins - metabolism Calponin calponin homology domain Calponins Cell signalling Cysteine - metabolism Cytoskeleton ELISA enzyme-linked immunosorbant sandwich assay ERK extracellular regulated kinase Fluorescent Dyes - metabolism Microfilament Proteins - metabolism Muscle Proteins - metabolism Muscle, Smooth - metabolism PKC Protein Binding protein kinase C Rabbits Spectrometry, Fluorescence |
| title | Calponin binds G-actin and F-actin with similar affinity |
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